Search Results

Overview

Uniprot IDQ15459
Protein NameSplicing factor 3A subunit 1
Gene NameSF3A1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
105 VSEFKEGKAQEPSAA
115 EPSAAIPKVMQQQQQ
396 VRKDYDPKASKPLPP
424 GEKIPASKMQEHMRI
486 VEETAIGKKIGEEEI
487 EETAIGKKIGEEEIQ
531 EQIEAIHKAKGLVPE
533 IEAIHKAKGLVPEDD
702 EEFLRRNKGPVSIKV

Function

Component of the 17S U2 SnRNP complex of the spliceosome, a large ribonucleoprotein complex that removes introns from transcribed pre-mRNAs (PubMed:10882114, PubMed:11533230, PubMed:32494006). The 17S U2 SnRNP complex (1) directly participates in early spliceosome assembly and (2) mediates recognition of the intron branch site during pre-mRNA splicing by promoting the selection of the pre-mRNA branch-site adenosine, the nucleophile for the first step of splicing (PubMed:10882114, PubMed:11533230, PubMed:32494006). Within the 17S U2 SnRNP complex, SF3A1 is part of the SF3A subcomplex that contributes to the assembly of the 17S U2 snRNP, and the subsequent assembly of the pre-spliceosome 'E' complex and the pre-catalytic spliceosome 'A' complex (PubMed:10882114, PubMed:11533230). Involved in pre-mRNA splicing as a component of pre-catalytic spliceosome 'B' complexes (PubMed:29360106, PubMed:30315277)

Protein Sequence

10 MPAGPVQAVP 20 PPPPVPTEPK 30 QPTEEEASSK 40 EDSAPSKPVV 50 GIIYPPPEVR 60 NIVDKTASFV 70 ARNGPEFEAR 80 IRQNEINNPK 90 FNFLNPNDPY 100 HAYYRHKVSE 110 FKEGKAQEPS 120 AAIPKVMQQQ 130 QQTTQQQLPQ 140 KVQAQVIQET 150 IVPKEPPPEF 160 EFIADPPSIS 170 AFDLDVVKLT 180 AQFVARNGRQ 190 FLTQLMQKEQ 200 RNYQFDFLRP 210 QHSLFNYFTK 220 LVEQYTKILI 230 PPKGLFSKLK 240 KEAENPREVL 250 DQVCYRVEWA 260 KFQERERKKE 270 EEEKEKERVA 280 YAQIDWHDFV 290 VVETVDFQPN 300 EQGNFPPPTT 310 PEELGARILI 320 QERYEKFGES 330 EEVEMEVESD 340 EEDDKQEKAE 350 EPPSQLDQDT 360 QVQDMDEGSD 370 DEEEGQKVPP 380 PPETPMPPPL 390 PPTPDQVIVR 400 KDYDPKASKP 410 LPPAPAPDEY 420 LVSPITGEKI 430 PASKMQEHMR 440 IGLLDPRWLE 450 QRDRSIREKQ 460 SDDEVYAPGL 470 DIESSLKQLA 480 ERRTDIFGVE 490 ETAIGKKIGE 500 EEIQKPEEKV 510 TWDGHSGSMA 520 RTQQAAQANI 530 TLQEQIEAIH 540 KAKGLVPEDD 550 TKEKIGPSKP 560 NEIPQQPPPP 570 SSATNIPSSA 580 PPITSVPRPP 590 TMPPPVRTTV 600 VSAVPVMPRP 610 PMASVVRLPP 620 GSVIAPMPPI 630 IHAPRINVVP 640 MPPSAPPIMA 650 PRPPPMIVPT 660 AFVPAPPVAP 670 VPAPAPMPPV 680 HPPPPMEDEP 690 TSKKLKTEDS 700 LMPEEEFLRR 710 NKGPVSIKVQ 720 VPNMQDKTEW 730 KLNGQVLVFT 740 LPLTDQVSVI 750 KVKIHEATGM 760 PAGKQKLQYE 770 GIFIKDSNSL 780 AYYNMANGAV 790 IHLALKERGG RKK

Gene Ontology

Classification GO ID Description
Cellular Component GO:0071013 catalytic step 2 spliceosome
Cellular Component GO:0016607 nuclear speck
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0005681 spliceosomal complex
Cellular Component GO:0005686 U2 snRNP
Cellular Component GO:0071005 U2-type precatalytic spliceosome
Cellular Component GO:0071004 U2-type prespliceosome
Cellular Component GO:0005684 U2-type spliceosomal complex
Molecular Function GO:0003723 RNA binding
Biological Process GO:0000389 mRNA 3'-splice site recognition
Biological Process GO:0045292 mRNA cis splicing, via spliceosome
Biological Process GO:0006397 mRNA processing
Biological Process GO:0000398 mRNA splicing, via spliceosome
Biological Process GO:0000387 spliceosomal snRNP assembly
Biological Process GO:1903241 U2-type prespliceosome assembly

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[3] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[4] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[5] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[6] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[7] Chao L, Xu Y, Yang Y, Ao X, Liang J. Identification of lactylation-related biomarkers for diagnosis, prognosis, and treatment responsiveness in triple-negative breast cancer.. World J Surg Oncol 24(1):77. 2026 Jan 22. PMID: 41566505.

[8] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.